Interactions between sodium dodecyl sulfate micelles and peptides during matrix-assisted laser desorption/ionization mass spectrometry (MALDI-MS) of proteolytic digests

Tummala, Rama; Green‐Church, Kari B.; Limbach, Patrick A.

doi:10.1016/j.jasms.2005.04.006

Cited by 13 publications

(12 citation statements)

References 36 publications

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“…Probably, this ionization process improvement is due to the presence of a higher number of protein sites available on the polypeptide chains surface, as a function of the oligomeric dissociation and partial protein unfolding, originated by the significant interaction between HbGp and CTAC at pH 7.0. Improvement of MALDI signals for hydrophobic peptides, obtained from digestion of several proteins, in the presence of surfactants has been also previously reported [34]. On the other hand, the intensity of the double-protonated peaks associated to the Linker and monomer chains is decreased, when compared with previous work focusing native HbGp in the absence of surfactants [12].…”

Section: Resultssupporting

confidence: 59%

“…In the surfactant concentration range used in this work, SDS decreases, but does not to prevent completely, the sample ionization process [34,36], which has been a problem found previously by other researchers employing this technique. The analysis by MALDI-TOF-MS allowed us to obtain spectrometric data of sufficient intensity to evaluate the surfactant effect upon HbGp, especially at 0.2 mM of SDS.…”

Section: Discussionmentioning

confidence: 71%

“…Besides that, a number of reports in the literature [21,28] demonstrates that the presence of surfactant, especially SDS, compromises both the signal-to-noise ratio and mass accuracy in MALDI-TOF-MS analysis. These limitations are assumed to arise due to the poor incorporation of the protein in the crystalline matrix since the protein-surfactant interaction is stronger than the protein-matrix one [33,34]. All these effects could be responsible for the absence of the peaks corresponding to CTAC-monomer d adducts in the double-protonated molecule (d 2+ ).…”

Section: Resultsmentioning

confidence: 99%

See 2 more Smart Citations

Interaction of giant extracellular Glossoscolex paulistus hemoglobin (HbGp) with ionic surfactants: A MALDI-TOF-MS study

Oliveira

Moreira

Tabak

2008

International Journal of Biological Macromolecules

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Section: Resultssupporting

confidence: 59%

Section: Discussionmentioning

confidence: 71%

Section: Resultsmentioning

confidence: 99%

See 1 more Smart Citation

Interaction of giant extracellular Glossoscolex paulistus hemoglobin (HbGp) with ionic surfactants: A MALDI-TOF-MS study

Oliveira

Moreira

Tabak

2008

International Journal of Biological Macromolecules

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“…This was not the case for solvent-based MALDI analysis using traditional acidic aqueous/organic solvent conditions, which resulted in severe over-representation of hydrophilic peptide (1)(2)(3)(4)(5)(6)(7)(8)(9)(10)(11) and provided no spectra for insoluble amphiphilic peptide even when present at 50% relative molar amount. Less accurate representation of components in mixtures by the traditional method appears to be a combination of poor dissolution of peptides in the solvent and preferential ionization of more hydrophilic peptides in the mixture.…”

mentioning

confidence: 99%

Solvent-free MALDI-MS for the analysis of β-amyloid peptides via the mini-ball mill approach: Qualitative and quantitative advances

Trimpin

Deinzer

2007

J. Am. Soc. Mass Spectrom.

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Manual and automated solvent-free mini-ball mill (MBM) matrix-assisted laser desorption/ ionization (MALDI) analysis of mixtures of ␤-amyloid peptides (1-11), (33-42), (1-42) and non-␤-amyloid component of Alzheimer's disease peptide yielded interpretable spectra for all of the peptides present regardless of their relative amounts in the samples. This was not the case for solvent-based MALDI analysis using traditional acidic aqueous/organic solvent conditions, which resulted in severe over-representation of hydrophilic peptide (1-11) and provided no spectra for insoluble amphiphilic peptide (1-42) even when present at 50% relative molar amount. Less accurate representation of components in mixtures by the traditional method appears to be a combination of poor dissolution of peptides in the solvent and preferential ionization of more hydrophilic peptides in the mixture. Consequently, only MBM provided a complete tryptic map of ␤-amyloid (1-42) compared to 67% coverage by traditional MALDI. Acetonitrile (0.1% TFA) led to improved coverage only at a 50% molar ratio of peptide (1-42), but also to a side product of (1-42), Met oxidation (amino acid 35), a phenomenon not observed in MBM MALDI analysis. Traditional MALDI analysis resulted in over-representation of hydrophilic soluble ␤-amyloid (1-11) in defined mixtures and autoproteolytic peptides of trypsin. In contrast, over-representation and under-representation were less pronounced in solvent-free MALDI in all of the investigated cases. Analysis of defined peptide and tryptic peptide mixtures showed that MBM MALDI yielded greater qualitative reliability, which also improved quantitative response relative to the solvent-based approach. (J Am Soc Mass Spectrom 2007, 18, 1533-1543) © 2007 American Society for Mass Spectrometry E vading solvent-mediated changes, e.g., segregation and side-reactions, to the sample while achieving excellent sensitivity and resolution using the solvent-free matrix-assisted laser desorption/ ionization (MALDI) mass spectrometry (MS) method are important advantages for the analysis of synthetic polymers and other large synthetic macromolecules even when solubility restrictions apply [1][2][3]. However, the method is potentially as important for the analysis of peptide molecules that in many cases are intractable, such as peptides derived from membrane proteins. The current study seeks to determine if the mini-ball mill (MBM) MALDI-MS method [4] can representatively analyze sample mixture components as well as or better than the conventional solvent-based MALDI method. A common case where mixture analysis is important is in analyzing components of a tryptic digest. ␤-Amyloid(1-42), (Scheme 1), comprises a particularly good test since its tryptic digests are expected to contain a mixture with components of widely varying hydrophobicity [5]. This solubility-restricted, aggregating biopolymer [6,7] is amphiphilic (Scheme 1), and has a hydrophilic N-and a hydrophobic C-terminus. ␤-Amyloid (1-42) is an enzymatic cleavage product of the amyloid-...

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“…In contrast, some research groups have reported that SDS aids the MALDI‐MS analysis 12–15. The MALDI signal intensity for the SDS‐containing protein solutions was recovered by raising the SDS concentration of the sample to above 0.3%, which is near its critical micelle concentration (CMC) 12.…”

mentioning

confidence: 97%

The effect of sodium dodecyl sulfate and anion‐exchange silica gel on matrix‐assisted laser desorption/ionization mass spectrometric analysis of proteins

Asanuma

Fukuzawa

Matsuda

et al. 2009

Rapid Comm Mass Spectrometry

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Sodium dodecyl sulfate (SDS), an anionic surfactant, is widely used in peptide and protein sample preparation. When the sample is analyzed by matrix-assisted laser desorption/ionization mass spectrometry (MALDI-MS), this surfactant can often cause signal suppression. We have previously reported an on-probe sample preparation method using a suspension of anion-exchange silica gel and sinapinic acid (i.e., gel-SA suspension) as a matrix, thereby greatly improving the MALDI signal detection of the protein solutions containing SDS. In this study, we found that a certain amount of SDS enhanced the MALDI signal intensity for protein samples. This effect was also observed when using sodium decyl sulfate and sodium tetradecyl sulfate instead of SDS. Furthermore, this on-probe sample preparation method using both SDS and the gel-SA suspension improved the detection limit of protein samples in the MALDI-MS analysis by about ten-fold as compared to that of protein samples without SDS and the gel-SA suspension. This method can be applied not only to the MALDI-MS analysis of samples containing SDS, but also to the examination of proteins at femtomole levels or insoluble proteins such as membrane proteins.

show abstract

Interactions between sodium dodecyl sulfate micelles and peptides during matrix-assisted laser desorption/ionization mass spectrometry (MALDI-MS) of proteolytic digests

Cited by 13 publications

References 36 publications

Interaction of giant extracellular Glossoscolex paulistus hemoglobin (HbGp) with ionic surfactants: A MALDI-TOF-MS study

Interaction of giant extracellular Glossoscolex paulistus hemoglobin (HbGp) with ionic surfactants: A MALDI-TOF-MS study

Solvent-free MALDI-MS for the analysis of β-amyloid peptides via the mini-ball mill approach: Qualitative and quantitative advances

The effect of sodium dodecyl sulfate and anion‐exchange silica gel on matrix‐assisted laser desorption/ionization mass spectrometric analysis of proteins

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